New Details of HCV NS3/4A Proteinase Functionality Revealed by a High-Throughput Cleavage Assay

@article{Shiryaev2012NewDO,
  title={New Details of HCV NS3/4A Proteinase Functionality Revealed by a High-Throughput Cleavage Assay},
  author={S. Shiryaev and Elliot R. Thomsen and P. Cieplak and E. Chudin and A. Cheltsov and M. Chee and I. Kozlov and A. Strongin},
  journal={PLoS ONE},
  year={2012},
  volume={7}
}
Background The hepatitis C virus (HCV) genome encodes a long polyprotein, which is processed by host cell and viral proteases to the individual structural and non-structural (NS) proteins. HCV NS3/4A serine proteinase (NS3/4A) is a non-covalent heterodimer of the N-terminal, ∼180-residue portion of the 631-residue NS3 protein with the NS4A co-factor. NS3/4A cleaves the polyprotein sequence at four specific regions. NS3/4A is essential for viral replication and has been considered an attractive… Expand
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